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. 1999 Dec 13;147(6):1237–1248. doi: 10.1083/jcb.147.6.1237

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© 1999 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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Steady state fractionation properties of the transfected AE1-3 and AE1-4 anion exchangers. MDCK cells transiently expressing the AE1-3 and AE1-4 anion exchangers, or a point mutant of AE1-4 that eliminates the single N-linked glycosylation site, AE1-4N638T, were detergent lysed and separated into soluble (S) and insoluble (I) fractions by centrifugation. Equivalent amounts of the soluble and insoluble fractions were separated on a 6% SDS polyacrylamide gel, transferred to nitrocellulose, and probed with an AE1-specific antibody. After washing, the blot was incubated with GAR-IgG conjugated to horseradish peroxidase, and immunoreactive species were detected by enhanced chemiluminescence. Molecular mass markers to the left correspond to phosphorylase b (97 kD), and fructose-6-P-kinase (84 kD).